Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli.
Cysteine 195 in isocitrate lyase from Escherichia coli has been replaced by directed mutagenesis. Substitution by Ser yields enzyme with a k(cat) that is 0.03% that of wild type, and substitution by Ala, Gly, Thr, or Val yields completely inactive enzyme. The present results are consistent with a functional role of Cys 195.
Rehman
A
A
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.
McFadden
B A
BA
D000409:Alanine / Q000235:genetics; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D003545:Cysteine / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D005998:Glycine / Q000235:genetics; D007522:Isocitrate Lyase / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000235:genetics; D013912:Threonine / Q000235:genetics; D014633:Valine / Q000235:genetics
D013912:Threonine; D012694:Serine; D007522:Isocitrate Lyase; D014633:Valine; D003545:Cysteine; D000409:Alanine; D005998:Glycine